Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The interactive effects of lima bean trypsin inhibitor (TI), hemagglutinin (Hgg) and cyanide (CN) when fed at the same degree of activity as found in the raw lima bean (RLB) were assessed in weanling rats using hepatic glutamate dehydrogenase (GLDH), isocitrate dehydrogenase (ICDH), ornithine carbamoyltransferase (OCT) and intestinal disaccharidases activities as the response criteria. Whereas RLB significantly (P less than 0.05) increased hepatic GLDH and decreased ICDH activities respectively, dietary CN, TI and Hgg whether acting individually or jointly had no significant influence on GLDH. Only the CN-containing diets significantly (P less than 0.05) elevated ICDH activity when compared with the control. Raw lima bean significantly (P less than 0.05) depressed OCT activity while neither the individual nor collective effects of these factors were significant. Dietary CN + TI + Hgg interaction depressed maltase activity to approximately the same extent as RLB in all the intestinal regions. These factors had neither individual nor collective effects on sucrase in the small intestine. Lactase activity in the small intestine was influenced only by the RLB diet, while CN + Hgg, and CN + TI + Hgg dietary combinations induced significant (P less than 0.05) elevations in the activities of cellobiase when compared with the control. Although synergism of action is indicated in a number of instances, it is suggested that these factors may need to combine with others within the bean, perhaps synergistically, to elicit comparable anti-nutritional influences as the RLB.
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PMID:The interactive effects of lima bean (Phaseolus lunatus) trypsin inhibitor, hemagglutinin and cyanide on some hepatic dehydrogenases, ornithine carbamoyltransferase and intestinal disaccharidases in weanling rats. 324 17

The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases.
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PMID:The effect of low temperatures on enzyme activity. 782 25